NMR illuminates intrinsic disorder.
NMR illuminates intrinsic disorder.
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DOI：
10.1016/j.sbi.2021.03.015
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发表时间：
2021-10
影响因子：
6.8
通讯作者：
Wright PE
中科院分区：
文献类型：
--
作者：
Dyson HJ;Wright PE
NMR长期以来一直是表征内在无序蛋白质（IDP）和内在无序区域（IDR）的工具。这种方法继续提供了丰富的见解，解决方案中的国内流离失所者的性质，特别是与其他生物物理方法，如小角散射，单分子荧光，EPR和质谱法相结合。近年来，在包含有序和无序结构域的蛋白质的研究以及包含单个或几个氨基酸的重复片段的有问题的序列的表征方面取得了实质性进展。这些序列与阿尔茨海默氏症、帕金森氏症和亨廷顿氏症等疾病有关，在这些疾病中，紊乱的蛋白质错误折叠成有害的淀粉样蛋白。NMR的创新应用为蛋白质聚集机制和IDP与其靶标相互作用的复杂性提供了新的见解。作为理解IDP和IDR的溶液结构集合、动力学行为和功能机制的基础，NMR继续被证明是无价的。
NMR has long been instrumental in the characterization of intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs). This method continues to offer rich insights into the nature of IDPs in solution, especially in combination with other biophysical methods such as small-angle scattering, single-molecule fluorescence, EPR and mass spectrometry. Substantial advances have been made in recent years in studies of proteins containing both ordered and disordered domains and in characterization of problematic sequences containing repeated tracts of a single or a few amino acids. These sequences are relevant to disease states such as Alzheimer’s, Parkinson’s and Huntington’s diseases, where disordered proteins misfold into harmful amyloid. Innovative applications of NMR are providing novel insights into mechanisms of protein aggregation and the complexity of IDP interactions with their targets. As a basis for understanding the solution structural ensembles, dynamic behavior, and functional mechanisms of IDPs and IDRs, NMR continues to prove invaluable.
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